ArticleMolecular biology of the cell2003
The yeast hnRNP-like protein Hrp1/Nab4 sccumulates in the cytoplasm after hyperosmotic stress: a novel Fps1-dependent response.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Insights into the Mechanism of Pre-mRNA Splicing of Tiny Introns from the Genome of a Giant CiliateInternational journal of molecular sciences · 2022Article
- The hnRNP-like Nab3 termination factor can employ heterologous prion-like domains in place of its own essential low complexity domain.PloS one · 2017Article
- Noncanonical transcript forms in yeast and their regulation during environmental stress.RNA (New York, N.Y.) · 2010Article
- Alternative 3' pre-mRNA processing in Saccharomyces cerevisiae is modulated by Nab4/Hrp1 in vivo.PLoS biology · 2007Article
- Transcript selection and the recruitment of mRNA decay factors for NMD in Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2005Review
- Functional specificity of shuttling hnRNPs revealed by genome-wide analysis of their RNA binding profiles.RNA (New York, N.Y.) · 2005Article
- A synthetic A tail rescues yeast nuclear accumulation of a ribozyme-terminated transcript.RNA (New York, N.Y.) · 2004Article
- Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p.Molecular and cellular biology · 2004Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Hrp1/Nab4 shuttling protein belongs to a family of RNA binding proteins that bind to nascent RNA polymerase II transcripts and form hnRNP complexes. Members of this family function in a staggering array of cellular activities, ranging from transcription and pre-mRNA processing in the nucleus to cytoplasmic mRNA translation and turnover. It has recently been recognized that the yeast stress response can include alterations in hnRNP-mediated mRNA export. We now report that the steady-state localization of Hrp1p rapidly shifts from the nucleus to the cytoplasm in response to osmotic stress. In contrast to a general stress response resulting in a transient relocation, Hrp1p redistribution is specific to hyperosmotic stress and is only reversed after stress removal. Hrp1p relocalization requires both the CRM1/XPO1 exportin and the FPS1 glycerol transporter genes but is independent of ongoing RNA transcription and protein arginine methylation. However, mutations in the high osmolarity glycerol and protein kinase C osmosensing pathways do not impact the Hrp1p hyperosmotic response. We present a working model for the cytoplasmic accumulation of Hrp1 and discuss the implications of this relocalization on Hrp1p function.
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Registered trials
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